Supramolecular Control over Split‐Luciferase Complementation
Abstract: Supramolecular split‐enzyme complementation restores enzymatic activity and allows for on–off switching. Split‐luciferase fragment pairs were provided with an N‐terminal FGG sequence and screened for complementation through host‐guest binding to cucurbit[8]uril (Q8). Split‐luciferase heterocomplex formation was induced in a Q8 concentration dependent manner, resulting in a 20‐fold upregulation of luciferase activity. Supramolecular split‐luciferase complementation was fully reversible, as revealed by using two types of Q8 inhibitors. Competition studies with the weak‐binding FGG peptide revealed a 300‐fold enhanced stability for the formation of the ternary heterocomplex compared to binding of two of the same fragments to Q8. Stochiometric binding by the potent inhibitor memantine could be used for repeated cycling of luciferase activation and deactivation in conjunction with Q8, providing a versatile module for in vitro supramolecular signaling networks.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Supramolecular Control over Split‐Luciferase Complementation ; volume:128 ; number:31 ; year:2016 ; pages:9045-9049 ; extent:5
Angewandte Chemie ; 128, Heft 31 (2016), 9045-9049 (gesamt 5)
- Urheber
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Bosmans, Ralph P. G.
Briels, Jeroen M.
Milroy, Lech‐Gustav
de Greef, Tom F. A.
Merkx, Maarten
Brunsveld, Luc
- DOI
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10.1002/ange.201602807
- URN
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urn:nbn:de:101:1-2022110106253461755186
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2025, 07:26 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Bosmans, Ralph P. G.
- Briels, Jeroen M.
- Milroy, Lech‐Gustav
- de Greef, Tom F. A.
- Merkx, Maarten
- Brunsveld, Luc
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